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toxiclipasyn

Understanding the balance between functional and deleterious interactions of alpha-synuclein with lipid bilayers

Total Cost €

0

EC-Contrib. €

0

Partnership

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 toxiclipasyn project word cloud

Explore the words cloud of the toxiclipasyn project. It provides you a very rough idea of what is the project "toxiclipasyn" about.

combination    techniques    isolated    molecules    switch    diseases    structures    atomic    composition    misfold    parkinson    modulate    stages    synuclein    fulfil    magnetic    shown    physiological    nuclear    aggregation    innovative    small    deleterious    hallmark    pathology    conformations    interactions    form    membrane    propensity    dichroism    vivo    neurodegenerative    responsible    fibril    amyloid    biological    nature    vitro    disease    ageing    electron    microscopy    native    equilibrium    solution    membranes    thorough    plasticity    proteins    functional    structural    kinetic    synaptic    resonance    bound    fluorescence    spectroscopy    function    effect    toxic    gene    dimensional    knock    biophysical    mice    interaction    protein    circumstances    modifications    thermodynamic    disordered    alpha    synthetic    bilayers    kinetics    intrinsically    structure    model    vesicles    lipid    interplay    diabetes    force    lipids    helical    circular    conformation    pd    brain    life   

Project "toxiclipasyn" data sheet

The following table provides information about the project.

Coordinator
DEUTSCHES ZENTRUM FUR NEURODEGENERATIVE ERKRANKUNGEN EV 

Organization address
address: SIGMUND FREUD STRASSE 27
city: BONN
postcode: 53127
website: www.dzne.de

contact info
title: n.a.
name: n.a.
surname: n.a.
function: n.a.
email: n.a.
telephone: n.a.
fax: n.a.

 Coordinator Country Germany [DE]
 Project website https://www.dzne.de/en/research/research-areas/fundamental-research/research-groups/di-monte/research-areasfocus/
 Total cost 171˙460 €
 EC max contribution 171˙460 € (100%)
 Programme 1. H2020-EU.1.3.2. (Nurturing excellence by means of cross-border and cross-sector mobility)
 Code Call H2020-MSCA-IF-2015
 Funding Scheme MSCA-IF-EF-ST
 Starting year 2017
 Duration (year-month-day) from 2017-05-01   to  2019-04-30

 Partnership

Take a look of project's partnership.

# participants  country  role  EC contrib. [€] 
1    DEUTSCHES ZENTRUM FUR NEURODEGENERATIVE ERKRANKUNGEN EV DE (BONN) coordinator 171˙460.00

Map

 Project objective

Proteins are among the most essential molecules of life. In order to fulfil their native function(s) they need to adopt a well-defined three-dimensional structure. However, under some circumstances, proteins can misfold and/or form toxic amyloid structures, which are the hallmark of a range of diseases including type 2 diabetes and neurodegenerative diseases. In particular, the small pre-synaptic protein, alpha-synuclein (AS), whose aggregation is the hallmark of Parkinson’s disease, can adopt in vivo and in vitro an intrinsically disordered conformation in solution and an alpha helical state when bound to membranes; the equilibrium between these two conformations has been shown to be important for its proposed native function, e.g. synaptic plasticity, and to modulate its kinetics of fibril formation. Here, I propose to investigate the physiological factors responsible for the switch between functional and deleterious interactions between membrane bilayers and AS due to ageing or disease using an innovative combination of biological, structural, thermodynamic and kinetic studies. In particular, I propose to use both synthetic lipid model systems and isolated synaptic vesicles to study the effect of ageing and the presence of lipids associated with Parkinson’s disease pathology on the nature of the interaction between AS and lipid bilayers. The synaptic vesicles will be isolated from the brain of mice at different ageing stages, as well as from mice carrying gene modifications or knock out related to PD. The interaction between AS and the vesicles will be studied using a range of biophysical techniques including circular dichroism, fluorescence and nuclear magnetic resonance spectroscopy, Atomic Force and Electron Microscopy. The aim of this study is to establish a thorough understanding of the interplay between changes in lipid composition and increased propensity of protein aggregation.

 Publications

year authors and title journal last update
List of publications.
2018 James W. P. Brown, Georg Meisl, Tuomas P. J. Knowles, Alexander K. Buell, Christopher M. Dobson, Céline Galvagnion
Kinetic barriers to α-synuclein protofilament formation and conversion into mature fibrils
published pages: 7854-7857, ISSN: 1359-7345, DOI: 10.1039/c8cc03002b
Chemical Communications 54/56 2019-09-25
2018 Ingrid M. van der Wateren, Tuomas P. J. Knowles, Alexander K. Buell, Christopher M. Dobson, Céline Galvagnion
C-terminal truncation of α-synuclein promotes amyloid fibril amplification at physiological pH
published pages: 5506-5516, ISSN: 2041-6520, DOI: 10.1039/c8sc01109e
Chemical Science 9/25 2019-09-25
2018 Michele Perni, Patrick Flagmeier, Ryan Limbocker, Roberta Cascella, Francesco A. Aprile, Céline Galvagnion, Gabriella T. Heller, Georg Meisl, Serene W. Chen, Janet R. Kumita, Pavan K. Challa, Julius B. Kirkegaard, Samuel I. A. Cohen, Benedetta Mannini, Denise Barbut, Ellen A. A. Nollen, Cristina Cecchi, Nunilo Cremades, Tuomas P. J. Knowles, Fabrizio Chiti, Michael Zasloff, Michele Vendruscolo, Christopher M. Dobson
Multistep Inhibition of α-Synuclein Aggregation and Toxicity in Vitro and in Vivo by Trodusquemine
published pages: 2308-2319, ISSN: 1554-8929, DOI: 10.1021/acschembio.8b00466
ACS Chemical Biology 13/8 2019-09-25
2018 Johnny Habchi, Sean Chia, Céline Galvagnion, Thomas C. T. Michaels, Mathias M. J. Bellaiche, Francesco Simone Ruggeri, Michele Sanguanini, Ilaria Idini, Janet R. Kumita, Emma Sparr, Sara Linse, Christopher M. Dobson, Tuomas P. J. Knowles, Michele Vendruscolo
Cholesterol catalyses Aβ42 aggregation through a heterogeneous nucleation pathway in the presence of lipid membranes
published pages: 673-683, ISSN: 1755-4330, DOI: 10.1038/s41557-018-0031-x
Nature Chemistry 10/6 2019-09-25

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